1n6t
From Proteopedia
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| - | [[Image:1n6t.jpg|left|200px]] | + | [[Image:1n6t.jpg|left|200px]] |
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| - | '''Solution Structure of the Tachykinin Peptide Neurokinin A''' | + | {{Structure |
| + | |PDB= 1n6t |SIZE=350|CAPTION= <scene name='initialview01'>1n6t</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution Structure of the Tachykinin Peptide Neurokinin A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1N6T is a [ | + | 1N6T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6T OCA]. |
==Reference== | ==Reference== | ||
| - | Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles., Chandrashekar IR, Cowsik SM, Biophys J. 2003 Dec;85(6):4002-11. PMID:[http:// | + | Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles., Chandrashekar IR, Cowsik SM, Biophys J. 2003 Dec;85(6):4002-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14645089 14645089] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chandrashekar, I R.]] | [[Category: Chandrashekar, I R.]] | ||
[[Category: Cowsik, S M.]] | [[Category: Cowsik, S M.]] | ||
[[Category: 3 10 helix]] | [[Category: 3 10 helix]] | ||
| - | [[Category: dpc | + | [[Category: dpc micelle]] |
[[Category: helix]] | [[Category: helix]] | ||
[[Category: lipid induced conformation]] | [[Category: lipid induced conformation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:56 2008'' |
Revision as of 10:52, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Structure of the Tachykinin Peptide Neurokinin A
Overview
The solution structure of NKA, a decapeptide of mammalian origin, has been characterized by CD spectropolarimetry and 2D proton nuclear magnetic resonance (2D 1H-NMR) spectroscopy in both aqueous and membrane mimetic solvents. Unambiguous NMR assignments of protons have been made with the aid of correlation spectroscopy (DQF-COSY and TOCSY) experiments and nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The distance constraints obtained from the NMR data have been utilized to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that in water NKA prefers to be in an extended chain conformation whereas a helical conformation is induced in the central core and the C-terminal region (D4-M10) of the peptide in the presence of perdeuterated dodecylphosphocholine (DPC) micelles, a membrane model system. Though less defined the N-terminus also displays some degree of order and a possible turn structure. The conformation adopted by NKA in the presence of DPC micelles represents a structural motif typical of neurokinin-2 selective agonists and is similar to that reported for eledoisin in hydrophobic environment.
About this Structure
1N6T is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles., Chandrashekar IR, Cowsik SM, Biophys J. 2003 Dec;85(6):4002-11. PMID:14645089
Page seeded by OCA on Thu Mar 20 12:52:56 2008
